View source for 5hiu


==Structure of the TSC2 N-terminus==
<StructureSection load='5hiu' size='340' side='right'caption='[[5hiu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hiu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HIU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hiu OCA], [https://pdbe.org/5hiu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hiu RCSB], [https://www.ebi.ac.uk/pdbsum/5hiu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hiu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G0SFF5_CHATD G0SFF5_CHATD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tuberous sclerosis complex (TSC) is caused by mutations in the TSC1 and TSC2 tumor suppressor genes. The gene products hamartin and tuberin form the TSC complex that acts as GTPase activating protein for Rheb and negatively regulates the mammalian target of rapamycin complex 1 (mTORC1). Tuberin contains a RapGAP homology domain responsible for inactivation of Rheb, but functions of other protein domains remain elusive. Here we show that the TSC2 N-terminus interacts with the TSC1 C-terminus to mediate complex formation. The structure of the TSC2 N-terminal domain from Chaetomium thermophilum and a homology model of the human tuberin N-terminus are presented. We characterize the molecular requirements for TSC1-TSC2 interactions and analyze pathological point mutations in tuberin. Many mutations are structural and produce improperly folded protein, explaining their effect in pathology, but we identify one point mutant that abrogates complex formation without affecting protein structure. We provide the first structural information on TSC2/tuberin with novel insight into the molecular function.

Structure of the Tuberous Sclerosis Complex 2 (TSC2) N-terminus Provides Insight into Complex Assembly and Tuberous Sclerosis Pathogenesis.,Zech R, Kiontke S, Mueller U, Oeckinghaus A, Kummel D J Biol Chem. 2016 Aug 4. pii: jbc.M116.732446. PMID:27493206<ref>PMID:27493206</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hiu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Chaetomium thermophilum]]
[[Category: Large Structures]]
[[Category: Kiontke S]]
[[Category: Kummel D]]
[[Category: Zech R]]